Abstract：
:The γ-aminobutyric acid type A receptor-associated protein (GABARAP) and its close paralogs GABARAPL1 and GABARAPL2 constitute a subfamily of the autophagy-related 8 (Atg8) protein family. Being associated with a variety of dynamic membranous structures of autophagic and non-autophagic origin, Atg8 proteins functionalize membranes by either serving as docking sites for other proteins or by acting as membrane tethers or adhesion factors. In this study, we describe that deficiency for GABARAP alone, but not for its close paralogs, is sufficient for accelerated EGF receptor (EGFR) degradation in response to EGF, which is accompanied by the downregulation of EGFR-mediated MAPK signaling, altered target gene expression, EGF uptake, and EGF vesicle composition over time. We further show that GABARAP and EGFR converge in the same distinct compartments at endogenous GABARAP expression levels in response to EGF stimulation. Furthermore, GABARAP associates with EGFR in living cells and binds to synthetic peptides that are derived from the EGFR cytoplasmic tail in vitro. Thus, our data strongly indicate a unique and novel role for GABARAP during EGFR trafficking.
journal_name
Cellsjournal_title
Cellsauthors
Dobner J,Simons IM,Rufinatscha K,Hänsch S,Schwarten M,Weiergräber OH,Abdollahzadeh I,Gensch T,Bode JG,Hoffmann S,Willbold Ddoi
10.3390/cells9051296subject
Has Abstractpub_date
2020-05-22 00:00:00issue
5issn
2073-4409pii
cells9051296journal_volume
9pub_type
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